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http://purl.uniprot.org/citations/15485655http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15485655http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15485655http://www.w3.org/2000/01/rdf-schema#comment"The control of cellular responses with fibroblast growth factors and neurotrophins is mediated through membrane-linked docking proteins, SNT (suc1-binding neurotrophic target)-1/FRS2alpha and SNT-2/FRS2beta. ERK1/2 are members of the mitogen-activated protein kinase family that regulate diverse cellular activities in response to various stimuli. Here, we demonstrate that SNT-2 does not become tyrosine phosphorylated significantly in response to EGF but forms a complex with ERK2 via the region of 186-252 amino acid residues, and the complex formation is enhanced upon EGF stimulation. SNT-2 downregulates ERK2 phosphorylation, suppresses and delays ERK2 nuclear accumulation which occurs following EGF stimulation. In contrast, the mutant SNT-2 which carries deletion of 186-252 amino acids and lacks ERK2 binding does not have these effects. These observations suggest that SNT-2 negatively regulates ERK2 signaling activated via EGF stimulation through direct binding to ERK2."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.09.152"xsd:string
http://purl.uniprot.org/citations/15485655http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.09.152"xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Huang L."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Huang L."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Shibuya M."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Shibuya M."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Tsuchida N."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Tsuchida N."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Gotoh N."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/author"Gotoh N."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/pages"1011-1017"xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/pages"1011-1017"xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/title"SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in response to EGF stimulation."xsd:string
http://purl.uniprot.org/citations/15485655http://purl.uniprot.org/core/title"SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in response to EGF stimulation."xsd:string